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Information on EC 1.3.8.6 - glutaryl-CoA dehydrogenase (ETF) and Organism(s) Mus musculus and UniProt Accession Q60759

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EC Tree
IUBMB Comments
Contains FAD. The enzyme catalyses the oxidation of glutaryl-CoA to glutaconyl-CoA (which remains bound to the enzyme), and the decarboxylation of the latter to crotonyl-CoA (cf. EC 7.2.4.5, glutaconyl-CoA decarboxylase). FAD is the electron acceptor in the oxidation of the substrate, and its reoxidation by electron-transfer flavoprotein completes the catalytic cycle. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (this entry), and a non-decarboxylating enzyme that only catalyses the oxidation to glutaconyl-CoA [EC 1.3.99.32, glutaryl-CoA dehydrogenase (acceptor)].
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Mus musculus
UNIPROT: Q60759
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
glutaryl-coa dehydrogenase, glutaryl-coenzyme a dehydrogenase, gdhgeo, glutaryl coenzyme a dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutaryl-CoA dehydrogenase
-
GCD
-
-
-
-
glutaryl coenzyme A dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
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redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
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dehydrogenation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
glutaryl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase (decarboxylating)
Contains FAD. The enzyme catalyses the oxidation of glutaryl-CoA to glutaconyl-CoA (which remains bound to the enzyme), and the decarboxylation of the latter to crotonyl-CoA (cf. EC 7.2.4.5, glutaconyl-CoA decarboxylase). FAD is the electron acceptor in the oxidation of the substrate, and its reoxidation by electron-transfer flavoprotein completes the catalytic cycle. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (this entry), and a non-decarboxylating enzyme that only catalyses the oxidation to glutaconyl-CoA [EC 1.3.99.32, glutaryl-CoA dehydrogenase (acceptor)].
CAS REGISTRY NUMBER
COMMENTARY hide
37255-38-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glutaryl-CoA + acceptor
crotonyl-CoA + CO2 + reduced acceptor
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.01
glutaryl-CoA
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.6
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glutaryl-CoA + electron-transfer flavoprotein
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cultured
Manually annotated by BRENDA team
additional information
-
distribution in various tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
injection of (3H)-labeled 3-hydroxyglutaric acid into 6 week-old Gcdh knockout mice, a model of glutaric aciduria type 1, reveal a low recovery in kidney, liver, or brain tissue that does not differ from control mice. Significant amounts of 3-hydroxyglutaric acid are found to be excreted via the intestinal tract. Exposure of knockout mice to a high protein diet leads to an encephalopathic crisis, vacuolization in the brain, and death after 4-5 days. Under these conditions, high amounts of injected 3H-3-hydroxyglutaric acid are found in kidneys of Gcdh knockout mice, whereas the radioactivity recovered in brain and blood is reduced. The data demonstrate that under conditions mimicking encephalopathic crises the blood-brain barrier appears to remain intact
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GCDH_MOUSE
438
0
48606
Swiss-Prot
Mitochondrion (Reliability: 1)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vamecq, J.; van Hoof, F.
Implication of a peroxisomal enzyme in the catabolism of glutaryl-CoA
Biochem. J.
221
203-211
1984
Mus musculus
Manually annotated by BRENDA team
Woontner, M.; Crnic, L.S.; Koeller, D.M.
Analysis of the expression of murine glutaryl-CoA dehydrogenase: in vitro and in vivo studies
Mol. Genet. Metab.
69
116-122
2000
Mus musculus
Manually annotated by BRENDA team
Vamecq, J.; de Hoffmann, E.; van Hoff, F.
Mitochondrial and peroxisomal metabolism of glutaryl-CoA
Eur. J. Biochem.
146
663-669
1985
Mus musculus
Manually annotated by BRENDA team
Keyser, B.; Glatzel, M.; Stellmer, F.; Kortmann, B.; Lukacs, Z.; Koelker, S.; Sauer, S.W.; Muschol, N.; Herdering, W.; Thiem, J.; Goodman, S.I.; Koeller, D.M.; Ullrich, K.; Braulke, T.; Muehlhausen, C.
Transport and distribution of 3-hydroxyglutaric acid before and during induced encephalopathic crises in a mouse model of glutaric aciduria type 1
Biochim. Biophys. Acta
1782
385-390
2008
Mus musculus (Q60759), Mus musculus
Manually annotated by BRENDA team